Kamaboko Gels Research Articles

Complex characterization and formation mechanism of scallop (Patinopecten yessoensis) protein hydrolysates/κ‐carrageenan/konjac gum composite gels

The combination of κ-Carrageenan (KC) and konjac gum (KGM) were introduced to examine the impact on gelation and microstructural behaviors of scallop male gonads hydrolysates (SMGHs) and the involvement of intermolecular forces. In terms of G' response of SMGHs/KGM/KC, it obviously enhanced by 3.6- and 108.5-fold than controls of KGM/KC and SMGHs/KC at 0.1Hz, accompanying increasing melting temperatures from 27.9 (KGM/KC) and 30.0 (SMGHs/KC) to 33.7°C (SMGHs/KGM/KC), respectively. Additionally, SMGHs/KGM/KC with decreasing relaxation time T23 and blue shift of hydroxyl group than controls suggested higher water retention capacity and ordered conformation. Moreover, SMGHs/KGM/KC formed compact networks with thick walls as reflected by cryo-SEM and showed rougher surface with more aggregation as reflected by AFM. Furthermore, electrostatic in couple with hydrophobic interactions were dominant interactions, while hydrogen bonds were involved in subordinately in SMGHs/KGM/KC. PRACTICAL APPLICATION: Scallop (Patinopecten yessoensis) male gonads are always discarded during processing despite high-protein content and edibility. In the current research, scallop male gonad hydrolysates (SMGHs) exhibited gelation behavior, which have a potential role in developing marine source protein as a functional food base such as kamaboko gels, can, sausage and spread and even delivery vehicles for bioactive compounds.

Formation and stability of electrostatic complexes formed between scallop female gonad protein isolates and sodium alginate: Influence of pH, total concentration, blend ratio, and ionic strength.

The complex coacervation between scallop (Patinopecten yessoensis) female gonad protein isolates (SFGPIs) and sodium alginate (SA) was determined by the turbidimetric method. The impact of pH, total biopolymer concentration, biopolymer blend ratio, and various salt ionic on the mechanisms governing the complex coacervation of SFGPIs-SA complexes were also investigated. For the SFGPIs:SA ratio of 2:1 without adding NaCl, insoluble and soluble complexes were observed at pH 5.8 (pHφ1 ) and pH 8.2 (pHc ) with the optimum biopolymer interactions appearing at pH 2.6 (pHopt ). The maximum turbidity value increased with the increment of the total biopolymer concentration from 0.37 to 1.83 until attaining the critical value (0.75%). As the blend ratios rose from 1:3 to 12:1, the critical pH values (pHc , pHφ1 , and pHopt ) moved to higher pH. Furthermore, the addition of NaCl led to a remarkable decrease in turbidity over the whole pH region in SFGPIs-SA complexes. Moreover, monovalent ions (Na+ and K+ ) had the same effect on the formation of the SFGPIs-SA complex, whereas the divalent cations (Mg2+ and Ca2+ ) lessened the complex formation in comparison with the monovalent ions. This study offers a methodological and theoretical basis for the design of complex SFGPIs-SA systems by understanding the complex coacervation under different conditions. PRACTICAL APPLICATION: In recent years, several protein-polysaccharides complexes have been widely applied in food and biological systems. Scallop (Patinopecten yessoensis) female gonads are deemed as good marine sources for developing protein matrices on account of their high protein content and nutrients. In our study, the effects of different conditions on the mechanisms governing the complex coacervation of SFGPI-SA mixtures were investigated, and the instability of the system could be overcome by understanding the conditions for SFGPIs/SA complex formation, which have a feasible role in developing marine source-protein as afunctional food base such as kamaboko gels, can, sausage, fat substitutes, and delivery vehicles for bioactive compounds.

Effects of tyndallization temperature on the sterility and quality of kamaboko

In this study, kamaboko gels were tyndallized at various temperatures and sterilization efficiency and impact on quality parameters were assessed. The microbiological, physical, and chemical properties of kamaboko gels were determined throughout the tyndallization process. Superior sterilization efficiency was achieved by tyndallization at a higher temperature; and the combination of heat-induced germination and thermal inactivation of spores was proposed as the main reason. The process had minimal effect on the color of gels. While tyndallized gels heated at 80 °C possessed superior physical properties, all gels showed impaired quality with the progress of heating cycles. Sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE) revealed that the cause of alterations in quality differed depending on the processing temperature. This study suggests that the sterility of products could be improved by increasing the processing temperature, time or number of heating cycle.

Intermolecular interaction in the hybrid gel of scallop (Patinopecten yessoensis) male gonad hydrolysates and κ-carrageenan.

Various bond disrupting agents including NaCl, GuHCl, urea, and SDS were introduced to investigate the intermolecular interactions between scallop (Patinopecten yessoensis) male gonad hydrolysates (SMGHs) and κ-carrageenan (κ-C), which were monitored by changes in rheological property, water distribution, conformation characterization and microstructure by using rheometer, low field-NMR relaxometry, Fourier transform infrared (FTIR) spectroscopy, cryo-scanning electron microscopy (cryo-SEM), and confocal laser scanning microscopy. The results showed that the bond disrupting agents deteriorated the rheological property of SMGHs/κ-C in a dose-dependent manner. Indeed, at the same concentration of 2 M, NaCl deteriorated the SMGHs/κ-C more obviously than GuHCl and urea. In addition, SMGHs/κ-C with bond disrupting agents possessed higher relaxation times including T21 and T23 , indicating the migration to free water direction of bound and free water. Moreover, the FITR results showed the red-shift in water regions (amide A and B bands), amide I and II bands, and indicated the breakdown of hydrogen bonds and electrostatic interactions, indicating a disordered structure in SMGHs/κ-C by various bond disrupting agents. Furthermore, cryo-SEM results showed the change of SMGHs/κ-C from a homogeneous network to a looser and ruptured one with larger void spaces, and indicated the disrupted and tattered microstructure of SMGHs/κ-C by various bond disrupting agents. Additionally, SMGHs/κ-C as well showed less aggregates stained by RITC by bond disrupting agents. These results suggest that electrostatic interactions would be mainly involved in the maintenance of SMGHs/κ-C gel network. This study could provide theoretical and methodological basis for hydrogel products with modified gel strength and microstructure by understanding the intermolecular interactions in gel system. PRACTICAL APPLICATION: Scallop (Patinopecten yessoensis) male gonads as a high-protein part of scallop, is usually discarded during processing despite its edibility. In recent years, scallop male gonads are regarded as good sources to develop protein matrices due to their high protein content and numerous nutrients. In this study, scallop male gonad hydrolysates (SMGHs) were obtained by trypsin-treated process. The considerable gelation behavior of SMGHs indicated that the SMGHs could be potentially utilized as a novel thickener and additive in production of kamaboko gels, can, sausage and spread with marine flavor.

Effect of Catla catla roe protein isolate on textural and sensorial properties of surimi gel from Piaractus brachypomus

Influence of protein isolate from catla (Catla catla) roe at different levels (0–8%, w/w) on the textural and sensorial properties of surimi gel from red-bellied pacu (Piaractus brachypomus) were studied. Protein isolate from catla roe (CRPI) was prepared and evaluated for trypsin inhibitory activity. Surimi gels added with CRPI were subjected to shear stress, texture profile analysis, color, SDS-PAGE, microstructure, water holding capacity and sensorial analysis. CRPI had trypsin inhibitory activity of 771.7 ± 12.57 unit/g. The CRPI effectively prevented the degradation of myosin heavy chain (MHC) in a concentration-dependent manner in both modori (65/90 °C) and kamaboko (40/90 °C) gels. Nevertheless, surimi gels incorporated with 6% CRPI (w/w) exhibited higher textural properties. This was witnessed by higher shear stress, hardness, springiness, cohesiveness, gumminess, chewiness, adhesiveness, fracture force, and water-holding capacity for both gels (P < 0.05). Furthermore, increasing CRPI levels (8%, w/w) showed a detrimental effect on gelation. The whiteness of modori and kamaboko gels slightly decreased with increasing CRPI levels (P < 0.05). The microstructure of modori and kamaboko gels added with 6% CRPI was more ordered and compact with fewer voids, demonstrating a preventive effect of CRPI on hydrolysis of myofibrillar proteins. Moreover, both gels added with 6% CRPI presented the higher texture and overall likeness scores than that of gels devoid of CRPI (P < 0.05). Therefore, CRPI could be used as an alternative additive to improve the textural properties of red-bellied pacu surimi by mitigating autolysis caused by endogenous proteinase or serve as a co-gelling agent or binder.

Physiochemical Properties and Functional Characteristics of Protein Isolates from the Scallop (Patinopecten yessoensis) Gonad.

Protein isolates were recovered from scallop (Patinopecten yessoensis) gonads to develop a novel functional matrix by investigating their physiochemical and functional properties. Scallop gonad protein isolates (SGPIs) were prepared from degreased scallop gonads (DSGs) by an alkali extraction and isoelectric solubilization/precipitation (ISP) process. The protein compositions of the SGPIs were mainly vitellogenin and beta-actin with molecular weights of 266 and 42kDa, respectively, as determined using Nano-liquid chromatography-mass/mass (Nano-LC-MS/MS). After the ISP process, the protein solubility of the SGPIs was significantly improved, and the surface hydrophobicity of SGPIs intensely increased by 1.1-fold, which were attributed to the exposure of aromatic residues such as phenylalanine, tyrosine, and tryptophan. However, the content of total/reactive sulfhydryl in SGPIs was decreased compared with that of DSGs. Meanwhile, the ISP process caused partial protein unfolding, as indicated by circular dichroism analysis, which exhibited a remarkable rise in the β-sheet content with a parallel decline in the α-helix and random coil contents (P < 0.05). SGPIs exhibited a better oil absorption capacity and foaming property than both DSGs and soybean protein isolates (SPIs). Moreover, the emulsifying capacity of SGPIs was greatly enhanced by the ISP process, which was superior to the effect of commercial SPIs and was ascribed to its favorable solubility as well as surface characteristics. PRACTICAL APPLICATION: During the processing of scallop (Patinopecten yessoensis) adductors, scallop gonad, a high-protein part, is usually discarded as processing by-products despite its edibility. In recent years, scallop gonads are regarded as good sources to develop protein matrices due to their high protein content and numerous nutrients. In this study, scallop gonad protein isolates (SGPIs) were isolated by isoelectric solubilization/precipitation (ISP) process. The preferable solubility, foaming property coupled with high emulsifying property of SGPIs indicated that the SGPIs could be potentially utilized as a good protein emulsifier and additives in production of kamaboko gels, hamburger patties, sausages, and pet foods.

Gel-Forming Ability of Rohu as Affected by Egg White Powder Addition

The gel-forming ability of rohu (Labeo rohita) mince with and without egg white powder (EW) was investigated. Gel from washed mince (washed gel) was prepared under two setting conditions: kamaboko (40°C) and modori (60°C). The gel-forming ability of kamaboko and modori gels was improved by the addition of EW at 2%. The autolytic inhibition of kamaboko gel was obtained in gel added with 2% EW, and 1% EW of modori gel. No marked change was observed in the TCA-soluble peptide content of either gel with the addition of EW above 1%. No effect on the whiteness of both gels was shown after the addition of EW. The addition of EW exhibited smaller cavities and a more compact fibrous network in microstructure.

Serine protease inhibitors from squid ovary: extraction and its effect on proteolysis and gel properties of surimi.

Serine protease inhibitors from squid ovary (SOSPI) were extracted using different extraction media and conditions. Optimal condition included 0.45M NaCl for 1h. After heat treatment at 70°C for 10min, the highest specific activity was obtained. Based on Sephadex G-75 gel filtration and activity staining, the major SOSPIs were present as monomer with molecular weight of 9.10 and 10.27kDa. Impact of SOSPI on autolysis of bigeye snapper surimi was studied. Myosin heavy chain was more retained with coincidentally lower trichloroacetic acid-soluble peptide content as the level of SOSPI increased. When SOSPI at various levels (0.5-3%) was added into surimi, the highest breaking force of both kamaboko and modori gels containing 1% SOSPI was obtained. However, SOSPI had no effect on deformation of kamaboko gel but slightly increased the deformation of modori gel. SOSPI increased water holding capacity of both kamaboko and modori gels in a dose dependent manner, as indicated by the lowered expressible moisture content. SOSPI had no effect on the whiteness of both gels. Thus SOSPI can be used as the protein additive in surimi for increasing breaking force.

Characteristics of Kamaboko from Catfish (Clarias Gariepinus) Surimi Processed with Carrot and Beet Root as Filler and Natural Food Colorants

The objective of the study was to investigate the effect of beet root and carrot as filler and natural food colourant on the chemical, physical and sensory properties of kamaboko. Kamaboko from catfish (Clarias gariepinus) surimi was processed with carrot (Daucus carota) and beet root (Beta vulgaris) at two concentrations (12 and 16% of surimi weight). Assesment was done on chemical (proximate, pH), physical (folding test, WHC, gel strength and breaking force) properties as well as sensory evaluation. The results showed that kamaboko gel processed using beet root had better performance than kamaboko gel processed using carrot. Kamaboko processed using beet root has protein content, folding test, water holding capacity, gel strength, breaking force, and sensory characteristics (appearance, colour, odor, texture, and taste) better than kamaboko processed with carrot. Increasing concentration of filler only affect on the gel strength and breaking force of kamaboko processed with beet root. The best characteristic of kamaboko was obtained from kamaboko processed using beet root with concentration of 12%. However, beet root was not recommended as colourant since the colour was not stable especially when stored at freezer.

Chemical interactions and gel properties of black carp actomyosin affected by MTGase and their relationships

Partial least squares regression (PLSR) was applied to evaluate and correlate chemical interactions (–NH2 content, S–S bonds, four non-covalent interactions) with gel properties (dynamic rheological properties and cooking loss (CL)) of black carp actomyosin affected by microbial transglutaminase (MTGase) at suwari and kamaboko stages. The G′ and CL were significantly enhanced by MTGase and their values in kamaboko gels were higher than those in suwari gels at the same MTGase concentration. The γ-carboxyamide and amino cross-links, catalyzed by MTGase, were constructed at suwari stage and contributed to the network formation, while disulfide bonds were formed not only in suwari gels but also in kamaboko gels, further enhancing the gel network. PLSR analysis revealed that 86.6–90.3% of the variation of G′ and 91.8–94.4% of the variation of CL were best explained by chemical interactions. G′ mainly depended on covalent cross-links and gave positive correlation. CL was positively correlated with covalent cross-links, but negatively related to non-covalent bonds, indicating that covalent bonds promoted water extrusion, whereas non-covalent bonds were beneficial for water-holding.

Effect of trypsin inhibitor in adzuki bean (Vigna angularis) on proteolysis and gel properties of threadfin bream (Nemipterus bleekeri)

Trypsin inhibitor (TI) from adzuki bean seed was partially purified by heat-treatment at 90 °C for 10 min and it was used to study the impact on proteolysis and gelling properties of threadfin bream (Nemipterus bleekeri). TI showed the inhibitory activity against sarcoplasmic proteinases and autolysis of threadfin bream mince and washed mince in a concentration dependent manner. TI was effective in proteolysis prevention as shown by more retained myosin heavy chain (MHC) on SDS-PAGE. Effect of TI (0.5, 1, 2 and 3 g/100 g) on the properties of threadfin bream surimi was also investigated. Breaking force and deformation of kamaboko gel increased as added levels of TI increased (p < 0.05). This was associated with lower levels of protein degradation, as evidenced by the decreased in trichloroacetic acid-soluble peptide content (p < 0.05). However, whiteness slightly decreased (p < 0.05) with increasing TI levels. Therefore, TI at an appropriate level could be an alternative food-grade inhibitor to improve gel properties of surimi.

魚肉練り製品の食感に及ぼす塩分濃度, 塩の粒径, 塩類および市販塩の種類の影響

魚肉練り製品の食感に及ぼす塩分濃度, 塩の粒径, 塩類および市販塩の種類の影響

Comparison of Chemical Composition and Textural Properties of Vinegar-cured and Thermal Commercial Kamaboko Gels

Comparison of Chemical Composition and Textural Properties of Vinegar-cured and Thermal Commercial Kamaboko Gels

Effect of organic salts on setting gels and their corresponding acids on kamaboko gels prepared from squid Todarodes pacificus mantle muscle

The present study evaluated the quality of setting gels prepared by adding sodium acetate, sodium gluconate, sodium citrate, and sodium succinate to Todarodes pacificus mantle muscle meat, and of the acid-induced kamaboko gels produced by soaking the setting gels in their corresponding acid solutions. The breaking strength was the lowest for the setting gel treated with sodium acetate. The pH values of the acid-induced kamaboko gels decreased when soaked in acid, whereas their moisture contents, whitenesses, and breaking strengths increased. The citric acid-induced kamaboko gel had the highest whiteness index and breaking strength among the gels. The sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) patterns did not show large differences among the gels, except for a low-intensity polymer band in the gluconic acid-induced kamaboko gel. Sodium citrate combined with citric acid yielded the best-quality acid-induced kamaboko gel among all the combinations, so this condition was used to study the effect of organic salt levels. The breaking strength increased when a sodium citrate level of up to 3% was used for the sodium citrate-treated setting gel, and 10% for the citric acid-induced kamaboko gel. The SDS-PAGE patterns did not differ among the sodium citrate levels. Egg white and microbial transglutaminase were necessary for citric acid-induced kamaboko gel production.

Effect of bambara groundnut protein isolate on autolysis and gel properties of surimi from threadfin bream (Nemipterus bleekeri)

Impact of bambara groundnut protein isolate (BGPI) on autolysis and gel properties of surimi from threadfin bream (Nemipterus bleekeri) was investigated. BGPI with trypsin inhibitory activity of 6356.3 ± 6.02 unit/g markedly increased (P < 0.05) the breaking force and deformation of modori gel as the levels used (0–3 g/100 g) increased. Nevertheless, only 0.25 g/100 g BGPI increased breaking force and deformation of kamaboko gel and increasing BGPI levels showed detrimental effect on gelation. Myosin heavy chain (MHC) was more retained when BGPI concentration increased, especially in modori gel. However, whiteness slightly decreased (P < 0.05) with increasing BGPI levels. Microstructure of kamaboko gel added with 0.25 g/100 g BGPI had finer and more ordered fibrillar structure than that without BGPI addition. Therefore, BGPI at an appropriate level could be an alternative food-grade inhibitor to improve gel properties of surimi.

Contribution of Sarcoplasmic Proteins to Myofibrillar Proteins Gelation

Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on. The myosin molecule is the major myofibrillar protein in gelation. It is believed that washing steps during the traditional surimi process play an important role in enhancing the gel properties of the resultant kamaboko by removing water-soluble (sarcoplasmic, Sp-P) proteins. By contrast, some researchers claim that retaining Sp-P or adding it into the surimi gel network not only does not interfere with the action of myofibrillar proteins during the sol-gel transition step but also improves the gel characteristics of the resultant kamaboko. It seems that retention of Sp-P or their addition into raw surimi does enhance the textural properties of kamaboko gel perhaps by functioning as a proteinase inhibitor, particularly against trypsin and trypsin-like proteinases but this depends on the type of applied surimi process. Among different types of Sp-P, it has been claimed that some proteins such as endogenous transglutaminase (TGase) play a more important role than other Sp-P in bond formation, by catalyzing the cross-linking of myosin heavy chain (MHC) molecules during low-temperature setting of surimi, resulting a more elastic kamaboko gel.

Gelling characteristics of surimi from yellow stripe trevally (Selaroides leptolepis)

Yellow stripe trevally (Selaroides leptolepis) is one of the abundant dark-fleshed fish species caught in Southern Thailand. However, the pelagic fish have high content of dark flesh associated with the high lipid and myoglobin contents contributing to the difficulties in making high-quality surimi. However, setting or heating at an appropriate temperature can improve the property of gel by avoiding the degradation but enhancing cross-linking of proteins. Therefore, the objective of this study was to investigate the gel-forming ability of surimi from yellow stripe trevally prepared under different heating conditions. Surimi gels were prepared under different heating conditions. Textural properties, whiteness, expressible moisture content, trichloroacetic acid (TCA)-soluble peptide content, protein pattern and microstructure of gels were determined. Additionally, the optimal temperature of muscle transglutaminase (TGase) was determined using monodansyl cadaverine incorporation method. Kamaboko gel with prior setting at 40°C (K40) exhibited the highest breaking force, followed by another kamaboko gel having setting temperature of 25°C, directly heated gel and modori gel, respectively (p < 0.05). For deformation, both kamaboko gels showed the lower values than both directly heated gel and modori gel (p < 0.05). The lowest expressible moisture content and whiteness were found in K40 sample (p < 0.05). The optimal temperature of yellow stripe trevally muscle transglutaminase was found to be 40°C. The highest TCA-soluble peptide content with decreased myosin heavy chain was found in modori surimi gel (p < 0.05). K40 sample had finer and more ordered fibrillar structure with smaller voids than other gels. Yellow stripe trevally could be used as the new raw material for surimi which yielded the gel with high deformation. Setting at 40°C is a promising means to improve the properties of surimi gel. Conversely, the incubation of sol at temperature close to 60°C should be avoided to prevent gel weakening.

Effects of CaCl2 on chemical interactions and gel properties of surimi gels from two species of carps

Effects of CaCl2 on chemical interactions, textural properties and expressible moisture content of suwari and kamaboko gels from yellowcheek carp and grass carp were investigated. And the correlations between the contents of chemical interactions and physical properties of surimi gels were analyzed. The contents of chemical interactions, especially non-disulfide covalent bonds, disulfide bonds and hydrophobic interactions of suwari and kamaboko gels, varied with addition concentration of CaCl2 and fish species. Suwari and kamaboko gels from yellowcheek carp exhibited higher breaking force, deformation and gel strength than these from grass carp. Surimi gels (suwari and kamaboko gels) from yellowcheek carp and grass carp exhibited their maximum gel strength when 40 mmol/kg and 100 mmol/kg CaCl2 was added, respectively. Addition of CaCl2 at high concentration resulted in low water holding capacity of surimi gels. Correlation analysis indicated that the contents of nonspecific associations, ionic bonds, hydrophobic interactions and sulfhydryl groups exhibited significant correlation with breaking force of surimi gels from yellowcheek carp and grass carp. Additionally, the content of non-disulfide covalent bonds had significant positive correlations with breaking force and expressible moisture of surimi gel from yellowcheek carp.

Effect of setting conditions on mechanical properties of acid-induced Kamaboko gel from squid Todarodes pacificus mantle muscle meat

Squid Todarodes pacificussuwari gels, set at various temperatures and times, and acid-induced kamaboko gel, which was prepared by soaking suwari gel in 5% acetic acid for 20 h, were studied to evaluate the mechanical properties that are affected by setting conditions. Unset squid meat paste did not form a gel when soaked in acetic acid. The breaking strength of both suwari gel and acid-induced kamaboko gel showed a tendency to increase with setting temperature and time. SDS-PAGE analysis of suwari gel and acid-induced kamaboko gel, which were set at various temperatures and times, showed that myosin heavy chain (MHC) was observed at 30°C only for the first hour. The intensity of the MHC band at 30°C gradually decreased with setting time, while the intensity of the polymer band gradually increased with setting time. These results suggest that the protein-protein bonds in suwari gel affect the final texture of acid-induced kamaboko gel. Based on the analysis of the mechanical properties, and in consideration of the fact that the purpose of this experiment was to reduce energy usage, the best setting condition was determined to be 40°C for 3 h.

COMBINATION EFFECTS OF WHEY PROTEIN CONCENTRATE AND CALCIUM CHLORIDE ON THE PROPERTIES OF GOATFISH SURIMI GEL

ABSTRACT Effect of whey protein concentrate (WPC) in combination with calcium chloride (50 mmol/kg) on the gel properties of surimi produced from goatfish (Mulloidichthys martinicus) was investigated. Breaking force and deformation of both kamaboko (40/90C) and modori (60/90C) gel increased with increasing WPC (0–3%) (P &lt; 0.05). Myosin heavy chain (MHC) band intensity of all gels was more retained as WPC concentration increased. The coincidental increase in water‐holding capacity was obtained, however, the whiteness was slightly decreased. At all levels of WPC added, kamaboko gels added with CaCl2 exhibited the superior properties to those without CaCl2 (P &lt; 0.05). On the other hand, CaCl2 addition resulted in the poorer gel properties of modori gel, regardless of WPC addition. The microstructure of surimi gels added with 3% WPC generally became denser and more ordered, compared with the control gel, irrespective of CaCl2 addition.PRACTICAL APPLICATIONSGoatfish is the new raw material for surimi production; however, it yields the gel with poor quality. The addition of WPC and CaCl2 at the appropriate levels can be a promising means to improve the gel quality via the inhibition of endogenous proteinases and the enhancement of setting phenomenon, respectively. As a consequence, surimi industry is able to produce surimi from goatfish with the quality equivalent to that of surimi from commonly used species. Thus, the greater benefit can be gained from goatfish, especially for the surimi industry.